The folding through the thylakoid membrane of the D-I herbicide binding polypeptide and of the homologous D-2 subunit of photosystem II is predicted from comparison of amino acid sequences and hydropathy index plots with the folding of the subunits L and M of a bacterial photosystem. As the function
Molecular topology of the Photosystem II chlorophyllabinding protein, CP 43: Topology of a thylakoid membrane protein
โ Scribed by Richard T. Sayre; Elizabeth A. Wrobel-Boerner
- Publisher
- Springer
- Year
- 1994
- Tongue
- English
- Weight
- 879 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0166-8595
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โฆ Synopsis
We have used antibodies generated against synthetic peptides to determine the topology of the 43 kD chlorophyll a binding protein (CP 43) of Photosystem II. Based on the pattern of proteolytic fragments detected (on western blots) by peptide specific antibodies, a six transmembrane span topological model, with the amino and carboxyl termini located on the stromal membrane surface, is predicted. This structure is similar to that predicted for CP 47, a PS II chlorophyll a binding protein (Bricker T (1990) Photosynth Res 24: 1-13). The model is discussed in reference to the possible location of chlorophyll binding sites.
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Thylakoid membranes retaining a high capacity to phosphorylate the D 1 protein of photosystem II but free from contamination by exogenous proteases have been prepared. Almost all the DI protein in this preparation is unphosphorylated, but it is almost completely phosphorylated by illumination in the